ID A0A3Q7TNN8_VULVU Unreviewed; 1956 AA.
AC A0A3Q7TNN8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN10A {ECO:0000313|RefSeq:XP_025856775.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025856775.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025856775.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025856775.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025856775.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-
CC dependent sodium ion permeability of excitable membranes. Assuming
CC opened or closed conformations in response to the voltage difference
CC across the membrane, the protein forms a sodium-selective channel
CC through which sodium ions may pass in accordance with their
CC electrochemical gradient. Plays a role in neuropathic pain mechanisms.
CC {ECO:0000256|ARBA:ARBA00025291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00036239};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.8/SCN10A subfamily. {ECO:0000256|ARBA:ARBA00006764}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR RefSeq; XP_025856775.1; XM_026000990.1.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc_dom.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF208; SODIUM CHANNEL PROTEIN TYPE 10 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 192..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 252..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 376..403
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 698..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 870..893
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1154..1172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1193..1209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1221..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1358..1376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1396..1419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1512..1530
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1542..1561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1597..1625
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1700..1723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 134..409
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 669..899
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 907..1148
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1152..1428
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1477..1733
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..1956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1956 AA; 219974 MW; 18194744569D7BDE CRC64;
MEFPFGSLET TNFRRFTPES LVEIEKRIAA KQAAKKAKGK HREQKDQEEK PRPQLDLKAC
NQLPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLDKGRT ISRFSATRAL WLFSPFNLIR
RTAIKVSVHS YPLWFSLFIT VTILVNCVGM TQTELPDRIE YVFTVIYTFE ALIKILARGF
CLNEFAYLRD PWNWLDFSVI TLAYIGEATA LRGISGLRTF RVLRALKTVS VIPGLKVIVG
ALIHSVRKLA DVTILTVFCL SVFALVGLQL FKGNLKNKCV KNCAALNETG NYSSYGKPDF
YYNKPGTSDP LLCGNGSDAG HCPKGYLCLK TSDNPDFNYT SFDSFAWAFL SLFRLMTQDS
WERLYQQTLR ASGKMYMVFF VLVIFLGSFY LVNLILAVVT MAYEEQNQAT IDEIEAKEKT
FQETLEMLRK EQEVLAALGI DTASLHSYNG SPLPSKNASE RMHRMKPRVS EGSTDDNKSP
QSDPYNQRRM SFLGLTSGRR RASHGSVFHF RTPCLDTSFP DGVTDDGVFP GDRESHRGSL
LLGGGTSQQG PLLRSPLPQP SNPGSGHGED GHSTLPTGEL APGGIEVSAF DAGQKKTFLS
AEYLNEPFPA QRAMSVVSIM TSVLEELEES ERRCPPCLTS FAQKYLIWEC CPTWVKLKTV
LFGIVTDPFA ELTITLCIVV NTVFMAMEHH GMSSAFEAML QIGNIVFTVF FTAEMVFKII
AFDPYYYFQK RWNIFDCIIV TVSLIELGAA RKGSLSVLRT FRLLRVFKLA KSWPTLNTLI
KIIGNSVGAL GNLTIILAII VFVFALVGKQ LLGENYRDNR RNISAPNEEW PRWHMHDFFH
SFLIVFRILC GEWIENMWAC MEVGQKSVCL ILFLTVMVLG NLVVLNLFIA LLLNSFSADN
LATPDEDGEV NNLQVALARI QAFGHRTKKA ICNFFTRPCL LPWPKAEPQL VVKLPLSSSK
AENHIAANAA VGSPRGLPVS RGLRDDHSDF ITNPNIWVSV PIAEGESDLD DLEEDGEEDS
QSSQQEAILQ GQEQLQVETC EGHMAPRSPG SGMSSEDLAS YVDEKWKDEA AAQAPAEGGD
DTSSSEGSTV DCLDPEEILR KIPELADDLE EPDDCFTEGC LRHCPCCKVD ISKFPWTVGW
QVRKTCYRIV EHSWFESFII FMILLSSGSL AFEDYHLDQK PTVKALLEYT DRVFTFIFVL
EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILQ YSDVASIKAL RTLRALRPLR
ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNFFAGKFGR CINKTNEYFS
LVPLSIVNNI SDCKYQNHTG SFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDA
RDVNLQPKWE DNVYMYLYFV IFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ
KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTKQAFD IVIMVLICLN MITMMVETDE
QSAEKTKILN KINQFFVAVF TGECVMKMFA LRHYYFTNGW NVFDFIVVVL SIGSLVFSVI
LTSLENYFSP TLFRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
IYSIFGMASF PHVSWEAGID DMFNFQTFAN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD
PNLPNSNGSR GNCGSPAVGI LFFTTYIIIS FLIVVNMYIA VILENFNVAT QESSEPLSED
DFDMFYETWE KFDPEATQFI TFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
CLDILFAFTK NVLGESGELD SLKANIEEKF MATNVSKTSY EPIATTLRWK QEDISATVIQ
KAYRSYVLHR SMTISNPPAV PRAEEAVPPP DEAFVEFMVN ENCALPDKSE TASAASFPPS
YDSVTRGLSD QINMSTSSSM QNEDEGTSNK VTAPGP
//